Crystallization (Comment) | Organism |
---|---|
unliganded enzyme, in complex with NADPH, and in complex with NADPH and pyrrole-2-carboxylate | Pseudomonas syringae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas syringae | Q4U331 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+ | Mobile domains I and II of protein change their conformations to produce the catalytic form. Preference for NADPH over NADH is explained by the cofactor binding site architecture | Pseudomonas syringae |
Subunits | Comment | Organism |
---|---|---|
dimer | crystallization data | Pseudomonas syringae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | preference for NADPH over NADH | Pseudomonas syringae | |
NADPH | preference for NADPH over NADH | Pseudomonas syringae |